ID D1CD35_THET1 Unreviewed; 342 AA. AC D1CD35; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 22-FEB-2023, entry version 80. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01976}; DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01976}; GN Name=pfp {ECO:0000256|HAMAP-Rule:MF_01976}; GN OrderedLocusNames=Tter_1794 {ECO:0000313|EMBL:ACZ42700.1}; OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1). OC Bacteria; Chloroflexi; Thermobaculum. OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ42700.1, ECO:0000313|Proteomes:UP000000323}; RN [1] {ECO:0000313|EMBL:ACZ42700.1, ECO:0000313|Proteomes:UP000000323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323}; RX PubMed=21304745; RA Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M., Tice H., RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Lu M., Brettin T., Detter J.C., Goker M., RA Tindall B.J., Beck B., McDermott T.R., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Cheng J.F.; RT "Complete genome sequence of 'Thermobaculum terrenum' type strain (YNP1)."; RL Stand. Genomic Sci. 3:153-162(2010). RN [2] {ECO:0000313|Proteomes:UP000000323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323}; RX DOI=10.4056/sigs.1153107; RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M., RA Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., RA Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M., RA Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J., RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.; RT "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T)."; RL Stand. Genomic Sci. 3:153-162(2010). CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the CC first committing step of glycolysis. Uses inorganic phosphate (PPi) as CC phosphoryl donor instead of ATP like common ATP-dependent CC phosphofructokinases (ATP-PFKs), which renders the reaction reversible, CC and can thus function both in glycolysis and gluconeogenesis. CC Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- CC PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. CC {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01976}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_01976}; CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000256|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC Mixed-substrate PFK group III subfamily. {ECO:0000256|HAMAP- CC Rule:MF_01976}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01976}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001825; ACZ42700.1; -; Genomic_DNA. DR RefSeq; WP_012875732.1; NC_013525.1. DR AlphaFoldDB; D1CD35; -. DR STRING; 525904.Tter_1794; -. DR EnsemblBacteria; ACZ42700; ACZ42700; Tter_1794. DR KEGG; ttr:Tter_1794; -. DR eggNOG; COG0205; Bacteria. DR HOGENOM; CLU_020655_0_0_0; -. DR OMA; TNRDNPF; -. DR OrthoDB; 9802503at2; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000000323; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.450; -; 1. DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 1. DR HAMAP; MF_01976; Phosphofructokinase_III; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR012003; ATP_PFK_prok-type. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR012829; Phosphofructokinase_III. DR InterPro; IPR035966; PKF_sf. DR PANTHER; PTHR13697:SF52; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3; 1. DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_01976}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01976}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01976}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01976}; Reference proteome {ECO:0000313|Proteomes:UP000000323}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01976}. FT DOMAIN 2..297 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT ACT_SITE 126 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 10 FT /ligand="diphosphate" FT /ligand_id="ChEBI:CHEBI:33019" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 102 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 124..126 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 161 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 168..170 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 221 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 266 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT BINDING 272..275 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT SITE 103 FT /note="Important for catalytic activity and substrate FT specificity; stabilizes the transition state when the FT phosphoryl donor is PPi; prevents ATP from binding by FT mimicking the alpha-phosphate group of ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" FT SITE 123 FT /note="Important for catalytic activity; stabilizes the FT transition state when the phosphoryl donor is PPi" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01976" SQ SEQUENCE 342 AA; 36855 MW; 628C628D7B1BA090 CRC64; MKVGVLTGGG DAPGLNAAIR AVVLSALSRG DEVVGFLDGW KGVQDNLTIP LDREWVQDIH EVGGTNLGTS RTNPMKSEDT MKAVENHFRE NGLDVLIAIG GDDTLSVAAE LDRRGFPVVG VPKTMDNDVP ETDYCIGFDT AVNRLMESID RLRTTSRSHH RVMVVEAMGR DAGWVAGFGG LAGGADVILV PEIEVDLDDV AQRLEKVRSR GRSYAIVVAA EGISFGEAQV PENAKTDAFG HVILAEKAVG ERLAQEIESR LGWETRSIQI GHLHRGGSPT AFDRILGTRY GEKAVELAHN NSFGQMVVLH GLDLTTVPLA QIAGKTKTLY PQFIELIQNL NA //